Evidence map›Paper›PMID 21725061›Full record

ArticleMolecular & cellular proteomics : MCP2011

CIN85 interacting proteins in B cells-specific role for SHIP-1.

Tom Büchse, Nikolaus Horras, Eva Lenfert, Gerald Krystal, Sandra Körbel, Michael Schümann, Eberhard Krause, Stefan Mikkat, Markus Tiedge

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Quantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunity.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Review
  9. Article
  10. Review
  11. Endocytosis of receptor tyrosine kinases.Cold Spring Harbor perspectives in biology · 2013
    Review
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Tom BüchseInstitute of Medical Biochemistry and Molecular Biology, Medical Faculty, University of Rostock, Schillingallee 70, 18057 Rostock, Germany. tom.buechse@med.uni-rostock.de
Nikolaus Horras
Eva Lenfert
Gerald Krystal
Sandra Körbel
Michael Schümann
Eberhard Krause
Stefan Mikkat
Markus Tiedge
University of Rostock · DELeibniz Association · DEBC Cancer Agency · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Cbl-interacting 85-kDa protein (CIN85) plays an important role as a negative regulator of signaling pathways induced by receptor tyrosine kinases. By assembling multiprotein complexes this versatile adaptor enhances receptor tyrosine kinase-activated clathrin-mediated endocytosis and reduces phosphatidylinositol-3-kinase-induced phosphatidylinositol-3,4,5-trisphosphate production. Here we report the expression of CIN85 in primary splenic B lymphocytes and the B-lymphoma cell lines WEHI 231 and Ba/F3. Cross-linking of the B cell antigen receptor resulted in an increased association of CIN85 with the ubiquitin ligase Cbl. Through a systematic pull-down proteomics approach we identified 51 proteins that interact with CIN85 in B cells, including proteins not shown previously to be CIN85-associated. Among these proteins, the SH2-containing inositol phosphatase 1 (SHIP-1) co-precipitated with both the full-length CIN85 and each of its three SH3 domains. We also showed that this association is constitutive and depends on a region of 79 amino acids near the carboxyl terminus of SHIP-1, a region rich in potential SH3 domain binding sites. Because SHIP-1 is a major negative regulator of the phosphatidylinositol-3-kinase pathway in lymphocytes, we hypothesize that the interaction between SHIP-1 and CIN85 might synergistically facilitate the down-regulation of phosphatidylinositol-3,4,5-trisphosphate levels.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBinding SitesB-LymphocytesCell Line, TumorGene Expression RegulationHumansInositol Polyphosphate 5-PhosphatasesJurkat CellsMaleMass SpectrometryMiceMice, Inbred C57BLMultiprotein ComplexesNeoplasm ProteinsNerve Tissue ProteinsAdaptor Proteins, Signal TransducingInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanInpp5d protein, mouseMultiprotein ComplexesNeoplasm ProteinsNerve Tissue Proteinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol 3-KinasePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProto-Oncogene Proteins c-cblRecombinant ProteinsSh3kbp1 protein, mouse

Identifiers

PMID21725061
PMCPMC3205855
OpenAlexW2162057795

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.